Abstract
The measurement of autoantibodies to thyroid-stimulating hormone receptor (TSHR) is important for the diagnosis of autoimmune thyroid disease such as Graves' disease (GD). Although TSHR from porcine thyroid membrane is commonly used for the measurement of TSHR autoantibodies (TRAb), recombinant human TSHR (hTSHR) remains ideal in terms of stable supply and species identity. Here we set out to express recombinant hTSHR on the lipid-bilayer surface of magnetic nanoparticles from a magnetotactic bacterium, Magnetospirillum magneticum AMB-1. Using a tetracycline-inducible expression system, we successfully overexpressed functional hTSHR on bacterial magnetic particles (BacMPs) in AMB-1 via an anchor protein specific for BacMPs. The overexpressed hTSHR was membrane integrated and possessed both ligand and autoantibody binding activity. Our data suggest that hTSHR-displayed BacMPs have potential as novel tools for ligand-receptor interaction analysis or for TRAb immunoassay in GD patients. © 2013 by the authors; licensee MDPI, Basel, Switzerland.
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Sugamata, Y., Uchiyama, R., Honda, T., Tanaka, T., Matsunaga, T., & Yoshino, T. (2013). Functional expression of thyroid-stimulating hormone receptor on nano-sized bacterial magnetic particles in magnetospirillum magneticum AMB-1. International Journal of Molecular Sciences, 14(7), 14426–14438. https://doi.org/10.3390/ijms140714426
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